S100A8 Antibody eFluor 660 50-9745-42 from Thermo Fisher Scientific

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Theranostics
January 01 2022

Fig 1: Fc?RIIB promotes gMDSCs generation from HPCs via Stat3 signaling. (A) Volcano plots of differentially expressed genes in HPCs from WT or Fc?RIIB KO mice at 14 days post-grafting of MC38 cells (adjusted P = 0.01 and fold change (FC) = 2), n = 4. (B) Signaling pathway enrichment analysis of differentially expressed genes. (C) Heatmap of differentially expressed genes that function as transcription factors involved in differentiation of HPCs into GMPs, n = 4. (D) Heatmap of differentially expressed genes in Jak-Stat signaling from WT or Fc?RIIB KO HPCs, n = 4. (E, F) WT or KO Mice were sacrificed at day 14 post-grafting, and tumor-infiltrating MDSCs were assessed for Stat3 (E) and S100A8 (F) expression; n =5. (G) WT mice BMs were treated with Veh (PBS), GM-CSF (20ng/mL) for 48 hrs, in the presence or absence of STAT3-IN-1 (GM-Stat3i, 1µM), and MDSCs proportion were analyzed. (H, I) Isolated Gr-1+ cells from BM were treated with GM-CSF (20ng/mL) for 48 hrs, in the presence or absence of STAT3-IN-1 (GM-Stat3i, 1µM), DCF-DA (H) and PD-L1 (I) expression were assessed using FCM; n = 4. (J, K) BM derived MDSCs were treated with STAT3-IN-1 (GM-Stat3i, 1µM) for 48 hrs, and then cocultured with CFSE-labeled CD8+ T lymphocytes isolated from WT mice (1:2) for 3 days, the production of IFN-? in CD8+ T cells (J, n = 4), anti-CD3 and anti-CD28 induced proliferation (K, n = 4) were measured by FCM; n = 4. Data are expressed as means ± SD. **P <0.01, by Mann-Whitney test.
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Immunity
February 19 2019

Fig 2: Butyrate Promotes Antimicrobial Activity in Macrophages via HDAC Inhibitory Function(A–C) Gene expression of hcar2 (A), ffar2 (B), and ffar3 (C) on flow cytometry sorted CD19+ B, CD8+ T, naive CD4+ T, memory CD4+ T, CD56+ CD3- NK cells, CD14+ monocytes, CD141+ DCs, and CD1c+ DCs from the blood of healthy donors. Each dot represents one donor.(D) Gentamicin protection assay on control and butyrate macrophages, or butyrate macrophages differentiated in the presence of butyrate with pertussis toxin (PT).(E) Protein expression of acetyled histone 3 (Ac-H3) and acetyled histone 4 (Ac-H4) in control and butyrate macrophages (data from 2 individual donors per condition).(F and G) Intra-cellular expression of tri-methylated lysine27 on histone 3 (3MeH3K27) (F) and acetylated lysine 27 on histone 3 (AcH3K27) (G) protein on control and butyrate macrophages by flow cytometry.(H, J, L, and N) Gentamicin protection assay on control macrophages, butyrate macrophages, and macrophages differentiated in the presence of valproate, phenylbutyrate (H), SAHA (J), TMP195, and tubacin (L), SBHA, 1-naphthohydroxamic acid (NA), or RGFP966 (N).(I, K, M, and O) Gene expression of S100A8 in control macrophages, butyrate macrophages, and macrophages differentiated in the presence of valproate, phenylbutyrate (I), SAHA (K), TMP195, and tubacin (M), SBHA, 1-naphthohydroxamic acid (NA), or RGFP966 (O).(P) Gentamicin protection assay in control and butyrate macrophages with and without HDAC3 siRNA-mediated gene silencing.(Q) Extracellular acidification rate in control and butyrate macrophages, as well as in RGFP966 and TMP195 treated macrophages. Data represent the mean of three biological replicates.For the gentamicin protection assay, the percentage of CFU (of control) was calculated from mean value for control group.Each dot represents one independent donor. For pairwise comparison Mann-Whitney U test was performed and for multiple group comparisons a one-way ANOVA (Kruskal-Wallis test) was performed. *p < 0.05, **p < 0.01, and ***p < 0.001.Please also see Figure S5E.
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Immunity
February 19 2019

Fig 3: Upregulation of Calprotectin in Macrophages Differentiated in Presence of Butyrate(A) t-SNE plots of significantly (BH adjusted p value < 0.05) butyrate-induced antimicrobial genes (S100A8, S100A9, S100A12, LYZ, and FCN1) at the single-cell level.(B) Gene expression of S100A8, S100A9, S100A12 at steady state in control and butyrate macrophages.(C) Quantification of calprotectin in the supernatant by ELISA.(D) Intra-cellular expression of S100A8 and S100A9 protein at steady state by flow cytometry.(E) Representative immunoblot of calprotectin and ß-actin at steady state from three donors.(F) Quantification of calprotectin expression at steady state.(G) Gentamicin protection assay against Salmonella performed on control and butyrate macrophages treated with scrambled siRNA or a mix of S100A8 and S100A9 siRNA.Each dot represents one donor. Statistical significance was determined using Mann-Whitney U test *p < 0.05, **p < 0.01 and ***p < 0.001.Please also see Figure S5.

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S100A8 Antibody eFluor 660

Thermo Fisher Scientific's S100A8 Antibody eFluor 660 is a Mouse monoclonal antibody. The S100A8 Antibody eFluor 660 was generated using S100A8 as the antigen. It reacts with Homo Sapiens, and Human. This antibody has been shown to work in applications such as: Flow Cytometry.

Theranostics

Immunity

Immunity

S100A8 Antibody eFluor 660 from Thermo Fisher Scientific

Thermo Fisher Scientific

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S100A8 Antibody eFluor 660 from Thermo Fisher Scientific

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